Oyster-derived peptides as pancreatic lipase inhibitors: Kinetics, molecular interactions, and gastrointestinal stability

In this study, oyster peptide sequences with potential inhibitory activity against pancreatic lipase were screened using molecular docking. Inhibition kinetics, ultraviolet and fluorescence spectroscopy, circular dichroism, and in vitro simulated digestion were employed to investigate the inhibitory mechanism and gastrointestinal stability of the peptides NGDAGMV (P-N) and EAGAGGL (P-E) on pancreatic lipase (PL). The results demonstrated that both P-N and P-E could effectively inhibit PL activity, with IC 50 values of 3.122 and 5.781 mmol/L, respectively. The inhibition type was non-competitive. P-N can alter the covalent structure of PL through charge interactions, hydrogen bonding, C-H bonds, pi -sulfur bonds, and pi -alkyl bonds. Meanwhile, P-E can efficiently quench the intrinsic fluorescence of PL and change its secondary structure primarily through static quenching mediated by salt bridges, hydrogen bonds, C-H bonds, and alkyl bonds. This study provides a theoretical basis for using oyster peptides as natural PL inhibitors.